时    间：2023年9月27日 (星期三) 12:40-14:00

地    点：农生学院创新楼（B楼）104会议室

主办单位：农生学院学科与科技办、农生学院青年教师联谊会

报告题目：基于DIA的磷酸化蛋白组学全面揭示I型酪蛋白激酶调控植物生长发育的功能

报告摘要：

蛋白磷酸化由蛋白激酶介导，广泛参与真核生物生长发育和环境响应的复杂信号网络。I型酪蛋白激酶（CK1）底物众多，在植物和哺乳动物的生理过程、细胞活动等过程中发挥重要调控作用，但CK1功能的全面揭示仍受限于内源底物的精准识别。系统分析CK1介导的磷酸化事件将有助于其内源底物和生理功能的揭示与阐明。该研究以一类植物CK1为代表，利用基于DIA的磷酸化蛋白组学分离了CK1依赖的磷酸化肽段、磷酸化蛋白，富集验证了CK1的新识别基序，预测分析了CK1在不同物种中的潜在底物和功能，为系统阐明和全面揭示CK1介导的磷酸化的功能研究提供了重要线索。

报告人简介：

【所在学科研究组研究方向】：

1 激素作用及磷脂-激素信号协同调控植物发育的分子机理

2 蛋白酶体及蛋白磷酸化参与植物发育的机制

3 水稻、马铃薯重要农业性状调控的遗传机制

【代表性著作】：

1. Qu L, Liu MY, Zheng LL, Xue HW. 2023. Data-Independent Acquisition-based global phosphoproteomics reveals diverse roles of AEL (Arabidopsis EL1-like) Casein kinase 1s in plant development. Science Bulletin 9: S2095–9273(23)00535–2. 
2. Qu L, Wei Z, Chen HH, Liu T, Liao K, Xue, HW. 2021. Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division. Plant physiology 187: 917–930. 
3. Qu L, Chu YJ, Lin WH, Xue HW. 2021. A secretory phospholipase D regulates rice heading time through hydrolyzing phosphatidylcholine. Plos Genetics 17: e1009905. 
4. Zhang F*, Qu L*, Gu, YC, et al. 2022. Resequencing and genome-wide association studies of autotetraploid potato. Molecular Horticulture 2: 6.
5. Qu L, Lin LB, Xue HW. 2019. Rice miR394 suppresses leaf inclination through targeting an F-box gene, LEAF INCLINATION 4. J Integrative Plant Biology 61: 406-416.
6. Chen HH, Qu L,Xu ZH,et al. 2018. EL1-like casein kinases suppress ABA signaling and responses by phosp horylating and destabilizing the ABA receptors PYR/PYLs in Arabidopsis. Molecular Plant 11: 706-19.

ACADEMIC SALON (XLI)

SPEAKER: Li QU

Postdoc, Department of Plant Science, SAB

TIME ：12:40-14:00  September 27th, 2023  (Wed)

VENUE：Room 104, Building B, SAB

ORGANIZER：Office of Discipline and Science & Technology, SAB;

  Young Teachers Association, SAB

TITLE：Data-Independent Acquisition-based global phosphoproteomics reveal the diverse roles of Casein kinase 1 in plant development

ABSTRACT：

Casein kinase 1s (CK1s) are serine/threonine protein kinases highly conserved among eukaryotes that regulate multiple developmental and signaling events through phosphorylation of target proteins. Arabidopsis early flowering 1 (EL1)-like (AELs) are plant-specific CK1s with varied functions, but identification and validation of their substrates is a major bottleneck in elucidating their physiological roles. Here, we conducted a quantitative phosphoproteomic analysis in data-independent acquisition mode to systematically enrich 3,985 phosphopeptides and identify 1,032 phosphoproteins. Furthermore, we searched the rice, mouse, and human protein databases using newly identified CK1 substrate motifs, yielding many more candidate substrates than currently known, largely expanding our understanding of the common and distinct functions exerted by CK1s in Arabidopsis and humans, facilitating future mechanistic studies of CK1-mediated phosphorylation in different species.